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The expanding world of oxidative protein folding

Nature Cell Biology volume 3, pages E247E249 (2001) | Download Citation

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An ever-expanding and diverse collection of proteins and small molecules is involved in the pathways leading to protein disulphide bond formation. However, the origin of oxidative power for this process in the eukaryotic endoplasmic reticulum has remained mysterious. It has now been shown that in the yeast endoplasmic reticulum (ER), the catalyst Erv2p, a member of the Erv1p/ALR protein family, uses molecular oxygen directly to contribute oxidizing equivalents for disulphide bond formation.

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Author information

Affiliations

  1. Hiroshi Kadokura and Jon Beckwith are at the Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA jbeckwith@hms.harvard.edu

    • Hiroshi Kadokura
    •  & Jon Beckwith

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DOI

https://doi.org/10.1038/ncb1101-e274b

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